Genetic dissection of a motility-associated c-di-GMP signalling protein of Pseudomonas putida
2013 (English)In: Environmental Microbiology Reports, ISSN 1758-2229, Vol. 5, no 4, 556-565 p.Article in journal (Refereed) Published
Lack of the Pseudomonas putidaPP2258 protein or its overexpression results in defective motility on solid media. The PP2258 protein is tripartite, possessing a PAS domain linked to two domains associated with turnover of c-di-GMP - a cyclic nucleotide that controls the switch between motile and sessile lifestyles. The second messenger c-di-GMP is produced by diguanylate cyclases and degraded by phosphodiesterases containing GGDEF and EAL or HD-GYP domains respectively. It is common for enzymes involved in c-di-GMP signalling to contain two domains with potentially opposing c-di-GMP turnover activities; however, usually one is degenerate and has been adopted to serve regulatory functions. Only a few proteins have previously been found to have dual enzymatic activities - being capable of both synthesizing and hydrolysing c-di-GMP. Here, using truncated and mutant derivatives of PP2258, we show that despite a lack of complete consensus in either the GGDEF or EAL motifs, the two c-di-GMP turnover domains can function independently of each other, and that the diguanylate cyclase activity is regulated by an inhibitory I-site within its GGDEF domain. Thus, motility-associated PP2258 can be added to the short list of bifunctional c-di-GMP signalling proteins.
Place, publisher, year, edition, pages
2013. Vol. 5, no 4, 556-565 p.
IdentifiersURN: urn:nbn:se:umu:diva-66137DOI: 10.1111/1758-2229.12045OAI: oai:DiVA.org:umu-66137DiVA: diva2:605793
FunderSwedish Research Council, 621-2008-3557Swedish Research Council, 2011-4791